Michael Sattler

The paper identifies miR-210-5p as a nuclear hypoxamiR that directly binds HIF-1 and enhances HIF-dependent transcription, revealing a new RNA-mediated regulatory mechanism.

This study identifies how DNA and ubiquitin relieve autoinhibition in SPRTN, enabling its protease activity through conformational changes.

The paper identifies PEX38 as a novel, essential peroxin in Euglenozoa, evolved from a remnant GET-pathway factor, and highlights its role in peroxisomal membrane protein targeting and potential as a therapeutic target.

This study identifies Sgt1 as an essential co-chaperone that stabilizes Hsp90-client complexes and prevents dissociation by Aha1, enhancing client maturation efficiency.

The paper introduces In-Pocket, a computational method that validates and improves the chemical accuracy of protein-ligand binding interfaces using quantum mechanics and experimental data.

This study identifies QKI as a regulator of splicing fidelity during cardiogenesis by interacting with U6 snRNA to enhance splicing at weak 5' splice sites.

The paper reports 37 new cases of RBM10 variants, identifies two phenotypic groups, and establishes a genotype-phenotype correlation based on functional studies.

The paper introduces a machine learning model that learns spatial preference maps for drug-receptor interactions to guide drug discovery.

The paper uses structural biology and computational methods to design MSI-1 mutants that alter RNA binding selectivity, validated by NMR and SPR experiments.

This study shows that ubiquitin activates SPRTN protease to degrade DNA-protein crosslinks, maintaining genome stability and preventing disease.

This study identifies PUN motifs in yeast Loc1p that cooperate to catalyze RNA folding and drive phase separation, suggesting a role in RNA and DNA-related processes across species.

The paper introduces MISATO, a dataset combining quantum mechanics properties and molecular dynamics simulations of protein-ligand complexes to support structure-based drug discovery.

This study shows that PURA syndrome mutations disrupt PURA's structure and P-body association, explaining full penetrance of the disease.

The paper identifies a splicing mechanism in human short introns involving RBM17 and SAP30BP, showing their interaction promotes splicing through a UHM-ULM binding and recruitment to phosphorylated SF3B1.

The paper identifies SPF45/RBM17 as essential for splicing a subset of human short introns, showing it competes with U2AF65 for binding to SF3B1, while U2AF is not required for this process.

The paper introduces a deep learning model called hotWater to predict water binding sites on protein surfaces using limited-resolution data, showing improved performance over existing methods.

The paper identifies the combinatorial RNA recognition code of IMP3 using an integrative approach combining SELEX-seq, iCLIP, and structural analysis.

This study reveals how hnRNP A1 binds to the terminal loop of pri-mir-18a, destabilizing stem base-pairing to enhance miRNA processing.